Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis

Thumbnail image of item number 1 in: 'Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis'.
Thumbnail image of item number 2 in: 'Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis'.
Thumbnail image of item number 3 in: 'Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis'.
Thumbnail image of item number 4 in: 'Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis'.
Showing 1-4 of 90 pages in this thesis.

PDF Version Also Available for Download.

Description

The enzyme, aspartate transcarbamoylase (ATCase) from Moraxella (Branhamella) catarrhalis, has been purified. The holoenzyme has a molecular mass of approximately 510kDa, harbors predominantly positive charges and is hydrophobic in nature. The holoenzyme possesses two subunits, a smaller one of 40 kDa and a larger one of 45 kDa. A third polypeptide has been found to contribute to the overall enzymatic activity, having an approximate mass of 55 kDa. The ATCase purification included the generation of cell-free extract, streptomycin sulfate cut, 60 °C heat step, ammonium sulfate cut, dialysis and ion, gel-filtration and hydrophobic interaction chromatography. The enzyme's performance throughout purification … continued below

Creation Information

Stawska, Agnieszka A. August 2001.

Context

This thesis is part of the collection entitled: UNT Theses and Dissertations and was provided by the UNT Libraries to the UNT Digital Library, a digital repository hosted by the UNT Libraries. It has been viewed 873 times. More information about this thesis can be viewed below.

Who

People and organizations associated with either the creation of this thesis or its content.

Author

Chair

Committee Members

Publisher

Rights Holder

For guidance see Citations, Rights, Re-Use.

  • Stawska, Agnieszka A.

Provided By

UNT Libraries

The UNT Libraries serve the university and community by providing access to physical and online collections, fostering information literacy, supporting academic research, and much, much more.

About | Browse this Partner

Contact Us

Corrections Questions

What

Descriptive information to help identify this thesis. Follow the links below to find similar items on the Digital Library.

Description

The enzyme, aspartate transcarbamoylase (ATCase) from Moraxella (Branhamella) catarrhalis, has been purified. The holoenzyme has a molecular mass of approximately 510kDa, harbors predominantly positive charges and is hydrophobic in nature. The holoenzyme possesses two subunits, a smaller one of 40 kDa and a larger one of 45 kDa. A third polypeptide has been found to contribute to the overall enzymatic activity, having an approximate mass of 55 kDa. The ATCase purification included the generation of cell-free extract, streptomycin sulfate cut, 60 °C heat step, ammonium sulfate cut, dialysis and ion, gel-filtration and hydrophobic interaction chromatography. The enzyme's performance throughout purification steps was analyzed on activity and SDS-PAGE gradient gels. Its enzymatic, specific activities, yield and fold purification, were also determined.

Language

Item Type

Identifier

Unique identifying numbers for this thesis in the Digital Library or other systems.

Collections

This thesis is part of the following collection of related materials.

UNT Theses and Dissertations

Theses and dissertations represent a wealth of scholarly and artistic content created by masters and doctoral students in the degree-seeking process. Some ETDs in this collection are restricted to use by the UNT community.

About | Browse this Collection

What responsibilities do I have when using this thesis?

Digital Files

When

Dates and time periods associated with this thesis.

Creation Date

  • August 2001

Added to The UNT Digital Library

  • Sept. 25, 2007, 10:38 p.m.

Description Last Updated

  • Oct. 9, 2008, 11:59 a.m.

Usage Statistics

When was this thesis last used?

Yesterday: 0
Past 30 days: 1
Total Uses: 873
More Statistics

Interact With This Thesis

Here are some suggestions for what to do next.

Start Reading

Thumbnail image of item number 1 in: 'Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis'.
Thumbnail image of item number 2 in: 'Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis'.
Thumbnail image of item number 3 in: 'Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis'.
Thumbnail image of item number 4 in: 'Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis'.

PDF Version Also Available for Download.

Citations, Rights, Re-Use

International Image Interoperability Framework

IIF Logo

We support the IIIF Presentation API

Links for Robots

Helpful links in machine-readable formats.

Archival Resource Key (ARK)

International Image Interoperability Framework (IIIF)

Metadata Formats

Images

URLs

Stats

Stawska, Agnieszka A. Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis, thesis, August 2001; Denton, Texas. (https://digital.library.unt.edu/ark:/67531/metadc2864/: accessed May 27, 2024), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; .

Back to Top of Screen